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Volumn 144, Issue 6, 2014, Pages 529-544

Crystal structure of the sodium-proton antiporter NhaA dimer and new mechanistic insights

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI PROTEIN; NHAA PROTEIN, E COLI; PROTEIN BINDING; PROTON; SODIUM; SODIUM PROTON EXCHANGE PROTEIN;

EID: 84918551154     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201411219     Document Type: Article
Times cited : (78)

References (82)
  • 5
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity rescaling
    • Bussi, G., D. Donadio, and M. Parrinello. 2007. Canonical sampling through velocity rescaling. J. Chem. Phys. 126:014101. http://dx.doi .org/10.1063/1.2408420
    • (2007) J. Chem. Phys. , vol.126
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography.
    • Collaborative Computational Project, Number 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Cryst. D50:760- 763. http://dx.doi.org/10.1107/S0907444994003112
    • (1994) Acta Cryst. , vol.D50 , pp. 760-763
  • 8
    • 0242693130 scopus 로고    scopus 로고
    • Bacterial membrane lipids: Where do we stand?
    • Cronan, J.E. 2003. Bacterial membrane lipids: Where do we stand? Annu. Rev. Microbiol. 57:203-224. http://dx.doi.org/10.1146/ annurev.micro.57.030502.090851
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 203-224
    • Cronan, J.E.1
  • 9
    • 84865071760 scopus 로고    scopus 로고
    • Bendix: intuitive helix geometry analysis and abstraction
    • Dahl, A.C.E., M. Chavent, and M.S.P. Sansom. 2012. Bendix: intuitive helix geometry analysis and abstraction. Bioinformatics. 28:2193- 2194. http://dx.doi.org/10.1093/bioinformatics/bts357
    • (2012) Bioinformatics. , vol.28 , pp. 2193- 2194
    • Dahl, A.C.E.1    Chavent, M.2    Sansom, M.S.P.3
  • 10
    • 19744376674 scopus 로고    scopus 로고
    • Global topology analysis of the Escherichia coli inner membrane proteome
    • Daley, D.O., M. Rapp, E. Granseth, K. Melén, D. Drew, and G. von Heijne. 2005. Global topology analysis of the Escherichia coli inner membrane proteome. Science. 308:1321-1323. http://dx.doi.org/ 10.1126/science.1109730
    • (2005) Science. , vol.308 , pp. 1321-1323
    • Daley, D.O.1    Rapp, M.2    Granseth, E.3    Melén, K.4    Drew, D.5    von Heijne, G.6
  • 11
    • 33746414364 scopus 로고    scopus 로고
    • Considerations for the refinement of low-resolution crystal structures
    • DeLaBarre, B., and A.T. Brunger. 2006. Considerations for the refinement of low-resolution crystal structures. Acta Crystallogr. D Biol. Crystallogr. 62:923-932. http://dx.doi.org/10.1107/ S0907444906012650
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 923-932
    • DeLaBarre, B.1    Brunger, A.T.2
  • 12
    • 78650186363 scopus 로고    scopus 로고
    • Lipidbook: A public repository for force-field parameters used in membrane simulations
    • Domanski, J., P.J. Stansfeld, M.S. Sansom, and O. Beckstein. 2010. Lipidbook: A public repository for force-field parameters used in membrane simulations. J. Membr. Biol. 236:255-258. http://dx.doi .org/10.1007/s00232-010-9296-8
    • (2010) J. Membr. Biol. , vol.236 , pp. 255-258
    • Domanski, J.1    Stansfeld, P.J.2    Sansom, M.S.3    Beckstein, O.4
  • 13
    • 0035955445 scopus 로고    scopus 로고
    • Green fluorescent protein as an indicator to monitor membrane protein overexpression in Escherichia coli
    • Drew, D.E., G. von Heijne, P. Nordlund, and J.W. de Gier. 2001. Green fluorescent protein as an indicator to monitor membrane protein overexpression in Escherichia coli. FEBS Lett. 507:220-224. http:// dx.doi.org/10.1016/S0014-5793(01)02980-5
    • (2001) FEBS Lett. , vol.507 , pp. 220-224
    • Drew, D.E.1    von Heijne, G.2    Nordlund, P.3    de Gier, J.W.4
  • 14
    • 33645454462 scopus 로고    scopus 로고
    • Optimization of membrane protein overexpression and purification using GFP fusions
    • Drew, D., M. Lerch, E. Kunji, D.J. Slotboom, and J.W. de Gier. 2006. Optimization of membrane protein overexpression and purification using GFP fusions. Nat. Methods. 3:303-313. http://dx.doi .org/10.1038/nmeth0406-303
    • (2006) Nat. Methods. , vol.3 , pp. 303-313
    • Drew, D.1    Lerch, M.2    Kunji, E.3    Slotboom, D.J.4    de Gier, J.W.5
  • 15
    • 80052068980 scopus 로고    scopus 로고
    • Structure of the membrane domain of respiratory complex I
    • Efremov, R.G., and L.A. Sazanov. 2011. Structure of the membrane domain of respiratory complex I. Nature. 476:414-420. http://dx.doi .org/10.1038/nature10330
    • (2011) Nature. , vol.476 , pp. 414-420
    • Efremov, R.G.1    Sazanov, L.A.2
  • 17
    • 0028101308 scopus 로고
    • + exchanger isoforms NHE1 and NHE3 exist as stable dimers in membranes with a high degree of specificity for homodimers
    • + exchanger isoforms NHE1 and NHE3 exist as stable dimers in membranes with a high degree of specificity for homodimers. J. Biol. Chem. 269:2589-2596.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2589-2596
    • Fafournoux, P.1    Noël, J.2    Pouysségur, J.3
  • 20
    • 81055154363 scopus 로고    scopus 로고
    • Arginine residues at internal positions in a protein are always charged
    • Harms, M.J., J.L. Schlessman, G.R. Sue, and B. García-Moreno. 2011. Arginine residues at internal positions in a protein are always charged. Proc. Natl. Acad. Sci. USA. 108:18954-18959. http://dx.doi .org/10.1073/pnas.1104808108
    • (2011) Proc. Natl. Acad. Sci. USA. , vol.108 , pp. 18954-18959
    • Harms, M.J.1    Schlessman, J.L.2    Sue, G.R.3    García-Moreno, B.4
  • 22
    • 76249103944 scopus 로고    scopus 로고
    • + antiporter lines the cation passage, and Asp65 is critical for pH activation of the antiporter
    • + antiporter lines the cation passage, and Asp65 is critical for pH activation of the antiporter. J. Biol. Chem. 285:2211-2220. http://dx.doi.org/10.1074/ jbc.M109.047134
    • (2010) J. Biol. Chem. , vol.285 , pp. 2211-2220
    • Herz, K.1    Rimon, A.2    Olkhova, E.3    Kozachkov, L.4    Padan, E.5
  • 23
    • 38749123962 scopus 로고    scopus 로고
    • P-LINCS: A parallel linear constraint solver for molecular simulation
    • Hess, B. 2008. P-LINCS: A parallel linear constraint solver for molecular simulation. J. Chem. Theory Comput. 4:116-122. http://dx.doi .org/10.1021/ct700200b
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 116-122
    • Hess, B.1
  • 25
    • 0032376126 scopus 로고    scopus 로고
    • Violin plots: A Box plot-density trace synergism
    • Hintze, J., and R.D. Nelson. 1998. Violin plots: A Box plot-density trace synergism. Am. Stat. 52:181-184.
    • (1998) Am. Stat. , vol.52 , pp. 181-184
    • Hintze, J.1    Nelson, R.D.2
  • 26
    • 80054991427 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of the bile acid sodium symporter ASBT
    • Hu, N.J., S. Iwata, A.D. Cameron, and D. Drew. 2011. Crystal structure of a bacterial homologue of the bile acid sodium symporter ASBT. Nature. 478:408-411. http://dx.doi.org/10.1038/nature10450
    • (2011) Nature. , vol.478 , pp. 408-411
    • Hu, N.J.1    Iwata, S.2    Cameron, A.D.3    Drew, D.4
  • 27
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • Humphrey, W., A. Dalke, and K. Schulten. 1996. VMD: Visual molecular dynamics. J. Mol. Graph. 14:33-38. http://dx.doi.org/ 10.1016/0263-7855(96)00018-5
    • (1996) J. Mol. Graph. , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 30
    • 79955092337 scopus 로고    scopus 로고
    • Large shifts in pKa values of lysine residues buried inside a protein
    • Isom, D.G., C.A. Castañeda, B.R. Cannon, and B. García-Moreno. 2011. Large shifts in pKa values of lysine residues buried inside a protein. Proc. Natl. Acad. Sci. USA. 108:5260-5265. http://dx.doi .org/10.1073/pnas.1010750108
    • (2011) Proc. Natl. Acad. Sci. USA. , vol.108 , pp. 5260-5265
    • Isom, D.G.1    Castañeda, C.A.2    Cannon, B.R.3    García-Moreno, B.4
  • 31
    • 33846191634 scopus 로고    scopus 로고
    • Halide, ammonium, and alkali metal ion parameters for modeling aqueous solutions
    • Jensen, K.P., and W.L. Jorgensen. 2006. Halide, ammonium, and alkali metal ion parameters for modeling aqueous solutions. J. Chem. Theory Comput. 2:1499-1509. http://dx.doi.org/10.1021/ ct600252r
    • (2006) J. Chem. Theory Comput. , vol.2 , pp. 1499-1509
    • Jensen, K.P.1    Jorgensen, W.L.2
  • 32
    • 0030841587 scopus 로고    scopus 로고
    • Electron-density map interpretation
    • Jones, T.A., and M. Kjeldgaard. 1997. Electron-density map interpretation. Methods Enzymol. 277:173-208. http://dx.doi.org/10.1016/ S0076-6879(97)77012-5
    • (1997) Methods Enzymol. , vol.277 , pp. 173-208
    • Jones, T.A.1    Kjeldgaard, M.2
  • 33
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • Jorgensen, W.L., J. Chandrasekhar, J.D. Madura, R.W. Impey, and M.L. Klein. 1983. Comparison of simple potential functions for simulating liquid water. J. Chem. Phys. 79:926-935. http://dx.doi .org/10.1063/1.445869
    • (1983) J. Chem. Phys. , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Madura, J.D.3    Impey, R.W.4    Klein, M.L.5
  • 35
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides
    • Kaminski, G.A., R.A. Friesner, J. Tirado-Rives, and W.L. Jorgensen. 2001. Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides. J. Phys. Chem. B. 105:6474-6487. http://dx.doi .org/10.1021/jp003919d
    • (2001) J. Phys. Chem. B. , vol.105 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 37
    • 0002906346 scopus 로고    scopus 로고
    • Around O. In International Tables for Crystallography, Volume F.
    • Crystallography of Biological Macromolecules. M.G. Rossmann and E. Arnold, editors. Kluwer Academic Publishers, Dordrecht.
    • Kleywegt, G.J., J.Y. Zou, M. Kjeldgaard, and T.A. Jones. 2001. Around O. In International Tables for Crystallography, Volume F. Crystallography of Biological Macromolecules. M.G. Rossmann and E. Arnold, editors. Kluwer Academic Publishers, Dordrecht. 497-506.
    • (2001) , pp. 497-506
    • Kleywegt, G.J.1    Zou, J.Y.2    Kjeldgaard, M.3    Jones, T.A.4
  • 39
    • 33847650845 scopus 로고    scopus 로고
    • + antiporter of Escherichia coli, at physiological pH
    • + antiporter of Escherichia coli, at physiological pH. Biochemistry. 46:2419- 2430. http://dx.doi.org/10.1021/bi602393s
    • (2007) Biochemistry. , vol.46 , pp. 2419- 2430
    • Kozachkov, L.1    Herz, K.2    Padan, E.3
  • 40
    • 33646446451 scopus 로고    scopus 로고
    • Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains
    • Kucerka, N., S. Tristram-Nagle, and J.F. Nagle. 2006. Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains. J. Membr. Biol. 208:193-202. http://dx.doi.org/10.1007/ s00232-005-7006-8
    • (2006) J. Membr. Biol. , vol.208 , pp. 193-202
    • Kucerka, N.1    Tristram-Nagle, S.2    Nagle, J.F.3
  • 41
    • 0033550299 scopus 로고    scopus 로고
    • Salt bridge stability in monomeric proteins
    • Kumar, S., and R. Nussinov. 1999. Salt bridge stability in monomeric proteins. J. Mol. Biol. 293:1241-1255. http://dx.doi.org/10.1006/ jmbi.1999.3218
    • (1999) J. Mol. Biol. , vol.293 , pp. 1241-1255
    • Kumar, S.1    Nussinov, R.2
  • 42
    • 0036708467 scopus 로고    scopus 로고
    • Relationship between ion pair geometries and electrostatic strengths in proteins
    • Kumar, S., and R. Nussinov. 2002. Relationship between ion pair geometries and electrostatic strengths in proteins. Biophys. J. 83:1595- 1612. http://dx.doi.org/10.1016/S0006-3495(02)73929-5
    • (2002) Biophys. J. , vol.83 , pp. 1595- 1612
    • Kumar, S.1    Nussinov, R.2
  • 43
    • 38049188238 scopus 로고    scopus 로고
    • + exchanger 1 (NHE1): Functional and clinical implications
    • + exchanger 1 (NHE1): Functional and clinical implications. J. Biol. Chem. 282:37854-37863. http://dx.doi .org/10.1074/jbc.M705460200
    • (2007) J. Biol. Chem. , vol.282 , pp. 37854-37863
    • Landau, M.1    Herz, K.2    Padan, E.3    Ben-Tal, N.4
  • 45
    • 84907286117 scopus 로고    scopus 로고
    • MemStar: A one-shot Escherichia coli-based approach for high-level bacterial membrane protein production
    • Lee, C., H.J. Kang, A. Hjelm, A.A. Qureshi, E. Nji, H. Choudhury, K. Beis, J.W. de Gier, and D. Drew. 2014. MemStar: A one-shot Escherichia coli-based approach for high-level bacterial membrane protein production. FEBS Lett. 588:3761-3769. http://dx.doi.org/ 10.1016/j.febslet.2014.08.025
    • (2014) FEBS Lett. , vol.588 , pp. 3761-3769
    • Lee, C.1    Kang, H.J.2    Hjelm, A.3    Qureshi, A.A.4    Nji, E.5    Choudhury, H.6    Beis, K.7    de Gier, J.W.8    Drew, D.9
  • 46
    • 28644432877 scopus 로고    scopus 로고
    • Very fast empirical prediction and rationalization of protein pKa values
    • Li, H., A.D. Robertson, and J.H. Jensen. 2005. Very fast empirical prediction and rationalization of protein pKa values. Proteins. 61:704- 721. http://dx.doi.org/10.1002/prot.20660
    • (2005) Proteins. , vol.61 , pp. 704- 721
    • Li, H.1    Robertson, A.D.2    Jensen, J.H.3
  • 48
    • 79959553432 scopus 로고    scopus 로고
    • + antiporter NhaA from Escherichia coli: An electrophysiological study
    • + antiporter NhaA from Escherichia coli: An electrophysiological study. J. Biol. Chem. 286:23570-23581. http://dx.doi.org/10.1074/jbc.M111 .230235
    • (2011) J. Biol. Chem. , vol.286 , pp. 23570-23581
    • Mager, T.1    Rimon, A.2    Padan, E.3    Fendler, K.4
  • 51
    • 79958185452 scopus 로고    scopus 로고
    • MDAnalysis: A toolkit for the analysis of molecular dynamics simulations
    • Michaud-Agrawal, N., E.J. Denning, T.B. Woolf, and O. Beckstein. 2011. MDAnalysis: A toolkit for the analysis of molecular dynamics simulations. J. Comput. Chem. 32:2319-2327. http://dx.doi.org/ 10.1002/jcc.21787
    • (2011) J. Comput. Chem. , vol.32 , pp. 2319-2327
    • Michaud-Agrawal, N.1    Denning, E.J.2    Woolf, T.B.3    Beckstein, O.4
  • 52
    • 84986440341 scopus 로고
    • SETTLE: An analytical version of the SHAKE and RATTLE algorithms for rigid water models
    • Miyamoto, S., and P.A. Kollman. 1992. SETTLE: An analytical version of the SHAKE and RATTLE algorithms for rigid water models. J. Comput. Chem. 13:952-962. http://dx.doi.org/10.1002/jcc .540130805
    • (1992) J. Comput. Chem. , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 53
    • 21244475101 scopus 로고    scopus 로고
    • Phosphatidylethanolamine- phosphatidylglycerol bilayer as a model of the inner bacterial membrane
    • Murzyn, K., T. Róg, and M. Pasenkiewicz-Gierula. 2005. Phosphatidylethanolamine- phosphatidylglycerol bilayer as a model of the inner bacterial membrane. Biophys. J. 88:1091-1103. http:// dx.doi.org/10.1529/biophysj.104.048835
    • (2005) Biophys. J. , vol.88 , pp. 1091-1103
    • Murzyn, K.1    Róg, T.2    Pasenkiewicz-Gierula, M.3
  • 54
    • 68049148763 scopus 로고    scopus 로고
    • Combined computational and biochemical study reveals the importance of electrostatic interactions between the "pH sensor" and the cation binding site of the sodium/proton antiporter NhaA of Escherichia coli
    • Olkhova, E., L. Kozachkov, E. Padan, and H. Michel. 2009. Combined computational and biochemical study reveals the importance of electrostatic interactions between the "pH sensor" and the cation binding site of the sodium/proton antiporter NhaA of Escherichia coli. Proteins. 76:548-559. http://dx.doi.org/10.1002/ prot.22368
    • (2009) Proteins. , vol.76 , pp. 548-559
    • Olkhova, E.1    Kozachkov, L.2    Padan, E.3    Michel, H.4
  • 55
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:307-326. http://dx.doi.org/10.1016/S0076-6879(97)76066-X
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 56
    • 50449090660 scopus 로고    scopus 로고
    • + antiporter
    • + antiporter. Trends Biochem. Sci. 33:435-443. http://dx.doi.org/10.1016/j.tibs.2008.06.007
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 435-443
    • Padan, E.1
  • 58
    • 59149095664 scopus 로고    scopus 로고
    • NhaA crystal structure: functional-structural insights
    • Padan, E., L. Kozachkov, K. Herz, and A. Rimon. 2009. NhaA crystal structure: functional-structural insights. J. Exp. Biol. 212:1593- 1603. http://dx.doi.org/10.1242/jeb.026708
    • (2009) J. Exp. Biol. , vol.212 , pp. 1593- 1603
    • Padan, E.1    Kozachkov, L.2    Herz, K.3    Rimon, A.4
  • 60
    • 0022964758 scopus 로고
    • Molecular genetics of membrane phospholipid synthesis
    • Raetz, C.R. 1986. Molecular genetics of membrane phospholipid synthesis. Annu. Rev. Genet. 20:253-291. http://dx.doi.org/10.1146/ annurev.ge.20.120186.001345
    • (1986) Annu. Rev. Genet. , vol.20 , pp. 253-291
    • Raetz, C.R.1
  • 61
    • 0038298731 scopus 로고    scopus 로고
    • Mechanism of the lamellar/inverse hexagonal phase transition examined by high resolution x-ray diffraction
    • Rappolt, M., A. Hickel, F. Bringezu, and K. Lohner. 2003. Mechanism of the lamellar/inverse hexagonal phase transition examined by high resolution x-ray diffraction. Biophys. J. 84:3111-3122. http://dx.doi.org/10.1016/S0006-3495(03)70036-8
    • (2003) Biophys. J. , vol.84 , pp. 3111-3122
    • Rappolt, M.1    Hickel, A.2    Bringezu, F.3    Lohner, K.4
  • 63
    • 0033606250 scopus 로고    scopus 로고
    • OPLS all-atom model for amines: Resolution of the amine hydration problem
    • Rizzo, R.C., and W.L. Jorgensen. 1999. OPLS all-atom model for amines: Resolution of the amine hydration problem. J. Am. Chem. Soc. 121:4827-4836. http://dx.doi.org/10.1021/ja984106u
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 4827-4836
    • Rizzo, R.C.1    Jorgensen, W.L.2
  • 64
    • 77649273913 scopus 로고    scopus 로고
    • Model-guided mutagenesis drives functional studies of human NHA2, implicated in hypertension
    • Schushan, M., M. Xiang, P. Bogomiakov, E. Padan, R. Rao, and N. Ben-Tal. 2010. Model-guided mutagenesis drives functional studies of human NHA2, implicated in hypertension. J. Mol. Biol. 396:1181-1196.
    • (2010) J. Mol. Biol. , vol.396 , pp. 1181-1196
    • Schushan, M.1    Xiang, M.2    Bogomiakov, P.3    Padan, E.4    Rao, R.5    Ben-Tal, N.6
  • 65
    • 0003545910 scopus 로고
    • Multivariate Density Estimation: Theory, Practice, and Visualization.
    • John Wiley & Sons, New York.
    • Scott, D.W. 1992. Multivariate Density Estimation: Theory, Practice, and Visualization. John Wiley & Sons, New York. 317 pp.
    • (1992) , pp. 317
    • Scott, D.W.1
  • 66
    • 41449119304 scopus 로고    scopus 로고
    • Coarse-grained MD simulations of membrane protein-bilayer self-assembly
    • Scott, K.A., P.J. Bond, A. Ivetac, A.P. Chetwynd, S. Khalid, and M.S.P. Sansom. 2008. Coarse-grained MD simulations of membrane protein-bilayer self-assembly. Structure. 16:621-630. http:// dx.doi.org/10.1016/j.str.2008.01.014
    • (2008) Structure. , vol.16 , pp. 621-630
    • Scott, K.A.1    Bond, P.J.2    Ivetac, A.3    Chetwynd, A.P.4    Khalid, S.5    Sansom, M.S.P.6
  • 69
    • 79960258119 scopus 로고    scopus 로고
    • Improved treatment of ligands and coupling effects in empirical calculation and rationalization of pKa values
    • Søndergaard, C.R., M.H.M. Olsson, M. Rostkowski, and J.H. Jensen. 2011. Improved treatment of ligands and coupling effects in empirical calculation and rationalization of pKa values. J. Chem. Theory Comput. 7:2284-2295. http://dx.doi.org/10.1021/ct200133y
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 2284-2295
    • Søndergaard, C.R.1    Olsson, M.H.M.2    Rostkowski, M.3    Jensen, J.H.4
  • 70
    • 78651247312 scopus 로고    scopus 로고
    • Benchmarking membrane protein detergent stability for improving throughput of high-resolution X-ray structures
    • Sonoda, Y., S. Newstead, N.J. Hu, Y. Alguel, E. Nji, K. Beis, S. Yashiro, C. Lee, J. Leung, A.D. Cameron, et al. 2011. Benchmarking membrane protein detergent stability for improving throughput of high-resolution X-ray structures. Structure. 19:17-25. http://dx .doi.org/10.1016/j.str.2010.12.001
    • (2011) Structure. , vol.19 , pp. 17-25
    • Sonoda, Y.1    Newstead, S.2    Hu, N.J.3    Alguel, Y.4    Nji, E.5    Beis, K.6    Yashiro, S.7    Lee, C.8    Leung, J.9    Cameron, A.D.10
  • 71
    • 79954524314 scopus 로고    scopus 로고
    • From coarse grained to atomistic: A serial multiscale approach to membrane protein simulations
    • Stansfeld, P.J., and M.S.P. Sansom. 2011. From coarse grained to atomistic: A serial multiscale approach to membrane protein simulations. J. Chem. Theory Comput. 7:1157-1166. http://dx.doi .org/10.1021/ct100569y
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 1157-1166
    • Stansfeld, P.J.1    Sansom, M.S.P.2
  • 72
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier, F.W. 2005. Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif. 41:207-234. http:// dx.doi.org/10.1016/j.pep.2005.01.016
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 74
    • 0027536509 scopus 로고
    • Proton-sodium stoichiometry of NhaA, an electrogenic antiporter from Escherichia coli
    • Taglicht, D., E. Padan, and S. Schuldiner. 1993. Proton-sodium stoichiometry of NhaA, an electrogenic antiporter from Escherichia coli. J. Biol. Chem. 268:5382-5387.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5382-5387
    • Taglicht, D.1    Padan, E.2    Schuldiner, S.3
  • 75
    • 67949120080 scopus 로고    scopus 로고
    • United atom lipid parameters for combination with the optimized potentials for liquid simulations all-atom force field
    • Ulmschneider, J.P., and M.B. Ulmschneider. 2009. United atom lipid parameters for combination with the optimized potentials for liquid simulations all-atom force field. J. Chem. Theory Comput. 5:1803-1813. http://dx.doi.org/10.1021/ct900086b
    • (2009) J. Chem. Theory Comput. , vol.5 , pp. 1803-1813
    • Ulmschneider, J.P.1    Ulmschneider, M.B.2
  • 76
    • 77949399840 scopus 로고    scopus 로고
    • Mechanism and kinetics of peptide partitioning into membranes from all-atom simulations of thermostable peptides
    • Ulmschneider, M.B., J.P.F. Doux, J.A. Killian, J.C. Smith, and J.P. Ulmschneider. 2010. Mechanism and kinetics of peptide partitioning into membranes from all-atom simulations of thermostable peptides. J. Am. Chem. Soc. 132:3452-3460. http://dx.doi .org/10.1021/ja909347x
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 3452-3460
    • Ulmschneider, M.B.1    Doux, J.P.F.2    Killian, J.A.3    Smith, J.C.4    Ulmschneider, J.P.5
  • 77
    • 80053306385 scopus 로고    scopus 로고
    • In silico partitioning and transmembrane insertion of hydrophobic peptides under equilibrium conditions
    • Ulmschneider, J.P., J.C. Smith, S.H. White, and M.B. Ulmschneider. 2011. In silico partitioning and transmembrane insertion of hydrophobic peptides under equilibrium conditions. J. Am. Chem. Soc. 133:15487-15495. http://dx.doi.org/10.1021/ja204042f
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 15487-15495
    • Ulmschneider, J.P.1    Smith, J.C.2    White, S.H.3    Ulmschneider, M.B.4
  • 78
    • 84951294736 scopus 로고    scopus 로고
    • Seaborn: statistical data visualization.
    • (accessed October 31, 2014).
    • Waskom, M. 2014. Seaborn: statistical data visualization. http:// web.stanford.edu/~mwaskom/software/seaborn/ (accessed October 31, 2014).
    • (2014)
    • Waskom, M.1
  • 80
    • 0034610788 scopus 로고    scopus 로고
    • Three-dimensional structure of the ion-coupled transport protein NhaA
    • Williams, K.A. 2000. Three-dimensional structure of the ion-coupled transport protein NhaA. Nature. 403:112-115. http://dx.doi.org/ 10.1038/47534
    • (2000) Nature. , vol.403 , pp. 112-115
    • Williams, K.A.1
  • 81
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn, M.D., M.N. Isupov, and G.N. Murshudov. 2001. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D Biol. Crystallogr. 57:122-133. http://dx.doi.org/10.1107/S0907444900014736
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 82
    • 75649151032 scopus 로고    scopus 로고
    • xia2: an expert system for macromolecular crystallography data reduction
    • Winter, G. 2010. xia2: an expert system for macromolecular crystallography data reduction. J. Appl. Cryst. 43:186-190. http://dx.doi .org/10.1107/S0021889809045701
    • (2010) J. Appl. Cryst. , vol.43 , pp. 186-190
    • Winter, G.1


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